ArticleThe Journal of biological chemistry2011
Metal-driven operation of the human large-conductance voltage- and Ca2+-dependent potassium channel (BK) gating ring apparatus.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 32 citations in OpenAlex.
- Cytochrome C-like Domain Within the Human BK Channel.International journal of molecular sciences · 2025Article
- BK Channel Gating Mechanisms: Progresses Toward a Better Understanding of Variants Linked Neurological Diseases.Frontiers in physiology · 2021Review
- Physiological Roles and Therapeutic Potential of CaFrontiers in molecular neuroscience · 2018Review
- Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017Review
- Interactions of divalent cations with calcium binding sites of BK channels reveal independent motions within the gating ring.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Oxidative modulation of voltage-gated potassium channels.Antioxidants & redox signaling · 2014Review
- Transduction of voltage and Ca2+ signals by Slo1 BK channels.Physiology (Bethesda, Md.) · 2013Review
- State-dependent FRET reports calcium- and voltage-dependent gating-ring motions in BK channels.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Relative transmembrane segment rearrangements during BK channel activation resolved by structurally assigned fluorophore-quencher pairing.The Journal of general physiology · 2012Article
- Barium ions selectively activate BK channels via the Ca2+-bowl site.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The contribution of RCK domains to human BK channel allosteric activation.The Journal of biological chemistry · 2012Article
- C-terminal acidic cluster is involved in Ca2+-induced regulation of human transient receptor potential ankyrin 1 channel.The Journal of biological chemistry · 2012Article
- Mg(2+) binding to open and closed states can activate BK channels provided that the voltage sensors are elevated.The Journal of general physiology · 2011Article
- Targeting BK (big potassium) channels in epilepsy.Expert opinion on therapeutic targets · 2011Review
- A BK (Slo1) channel journey from molecule to physiology.Channels (Austin, Tex.)Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Large-conductance voltage- and Ca(2+)-dependent K(+) (BK, also known as MaxiK) channels are homo-tetrameric proteins with a broad expression pattern that potently regulate cellular excitability and Ca(2+) homeostasis. Their activation results from the complex synergy between the transmembrane voltage sensors and a large (>300 kDa) C-terminal, cytoplasmic complex (the "gating ring"), which confers sensitivity to intracellular Ca(2+) and other ligands. However, the molecular and biophysical operation of the gating ring remains unclear. We have used spectroscopic and particle-scale optical approaches to probe the metal-sensing properties of the human BK gating ring under physiologically relevant conditions. This functional molecular sensor undergoes Ca(2+)- and Mg(2+)-dependent conformational changes at physiologically relevant concentrations, detected by time-resolved and steady-state fluorescence spectroscopy. The lack of detectable Ba(2+)-evoked structural changes defined the metal selectivity of the gating ring. Neutralization of a high-affinity Ca(2+)-binding site (the "calcium bowl") reduced the Ca(2+) and abolished the Mg(2+) dependence of structural rearrangements. In congruence with electrophysiological investigations, these findings provide biochemical evidence that the gating ring possesses an additional high-affinity Ca(2+)-binding site and that Mg(2+) can bind to the calcium bowl with less affinity than Ca(2+). Dynamic light scattering analysis revealed a reversible Ca(2+)-dependent decrease of the hydrodynamic radius of the gating ring, consistent with a more compact overall shape. These structural changes, resolved under physiologically relevant conditions, likely represent the molecular transitions that initiate the ligand-induced activation of the human BK channel.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.